A series of sequential polypeptides, (Lys,-Ala,),, and random copolypeptides, (Lysx, Alay),, were synthesized. The competitive effect of Ala, a helix former, and Lys, whose homopolymer has a 0-form in neutral NaDodS04 solution, was determined by CD and absorption spectroscopy. All the polypeptides s
Conformation of sequential and random lysine–phenylalanine copolypeptides
✍ Scribed by Gerhard Seipke; Hans-Adolf Arfmann; Karl G. Wagner
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1980
- Tongue
- English
- Weight
- 681 KB
- Volume
- 19
- Category
- Article
- ISSN
- 0006-3525
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## Abstract The conformation of three sequential copolypeptides, poly(L‐tyrosyl‐L‐lysine), poly(L‐tyrosyl‐L‐lysyl‐L‐lysine), and poly[L‐tyrosyl‐(L‐lysyl)~2~‐L‐lysine] have been studied by a variety of techniques, including CD, ir spectroscopy, analytical ultracentrifugation, and x‐ray diffraction.
351 00 Padova, Ilaly synopsis Circular Dichroism measurements have been carried out on poly-L-lysine (PLL) and on random copolymers of lysine and phenylalanine a t various pH values and in the presence of different amounts of NaClOr. The results indicate that either the homopolymer or the copolymers
## Abstract Summary: The present study describes the synthesis of novel polypeptides containing __O__‐phospho‐L‐threonine [Thr(PO~3~H~2~)] and L‐aspartic acid. Random copolypeptides copoly[Thr(PO~3~H~2~)^__X__^Asp^__Y__^] (__X__:__Y__ = 25:75, 50:50, 75:25), were conventionally prepared by copolyme
To account for the relative contributions of lysine and alanine residues to the stability of alpha-helices of copolymers of these two residues, conformational energy calculations were carried out for several hexadecapeptides at several pHs. All the calculations considered explicitly the coupling bet